Evidence map›Paper›PMID 16525042›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006

Alternative splicing of the voltage-gated Ca2+ channel beta4 subunit creates a uniquely folded N-terminal protein binding domain with cell-specific expression in the cerebellar cortex.

Andrew C Vendel, Mark D Terry, Amelia R Striegel, Nicole M Iverson, Valerie Leuranguer, Christopher D Rithner, Barbara A Lyons, Gary E Pickard, Stuart A Tobet, William A Horne

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.9field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. A Tripartite Interaction Among the Calcium Channel αFrontiers in cellular neuroscience · 2019
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Regulation of high-voltage-activated CaWiley interdisciplinary reviews. Membrane transport and signaling · 2013
    Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Andrew C VendelDepartment of Biomedical Sciences, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado 80526, USA.
Mark D Terry
Amelia R Striegel
Nicole M Iverson
Valerie Leuranguer
Christopher D Rithner
Barbara A Lyons
Gary E Pickard
Stuart A Tobet
William A Horne
New Mexico State University · USColorado State University · US

Funding

REGULATION OF MEMBRANE EXCITABILITYR01NS024444 · NINDS · UNIVERSITY OF COLORADO DENVER · PI BEAM, KURT G · 1986 to 2005
$1.8M
Retinal Neurons Afferent to the Circadian SystemR01MH062296 · NIMH · COLORADO STATE UNIVERSITY-FORT COLLINS · PI PICKARD, GARY EDWARD · 2001 to 2005
$1.6M
MECHANISMS OF GNRH NEURON MIGRATION DURING DEVELOPMENTR01HD033441 · NICHD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SCHWARTING, GERALD A · 1997 to 2004
$1.5M
Calcium Channel Gating: It Matters How You Splice It.R01NS042600 · NINDS · CORNELL UNIVERSITY · PI HORNE, WILLIAM ALAN · 2003 to 2006
$1.1M
NICHD NIH HHS HD33441NIMH NIH HHS MH62296NINDS NIH HHS NS24444NINDS NIH HHS NS42600
6 · The paper itself

Abstract

Ca2+ channel beta subunits regulate cell-surface expression and gating of voltage-dependent Ca2+ channel alpha1 subunits. Based on primary sequence comparisons, beta subunits are predicted to be modular structures composed of five domains (A-E) that are related to the large family of membrane-associated guanylate kinase proteins. The crystal structure of the beta subunit core B-D domains has been reported recently; however, little is known about the structures of the A and E domains. The N-terminal A domain differs among the four subtypes of Ca2+ channel beta subunits (beta1-beta4) primarily as the result of two duplications of an ancestral gene containing multiple alternatively spliced exons. At least nine A domain sequences can be generated by alternative splicing. In this report, we focus on one A domain sequence, the highly conserved beta4a A domain. We solved its three-dimensional structure and show that it is expressed in punctate structures throughout the molecular layer of the cerebellar cortex. We also demonstrate that it does not participate directly in Cav2.1 Ca2+ channel gating but serves as a binding site in protein-protein interactions with synaptotagmin I and the LC2 domain of microtubule-associated protein 1A. With respect to beta4 subunits, the interactions are specific for the beta4a splice variant, because they do not occur with the beta4b A domain. These results have strong bearing on our current understanding of the structure of alternatively spliced Ca2+ channel beta subunits and the cell-specific roles they play in the CNS.

Indexed as

Alternative SplicingAnimalsBlotting, WesternCalcium ChannelsCerebellumDose-Response Relationship, RadiationElectric StimulationGene ExpressionGene LibraryHumansImmunohistochemistryIon Channel GatingMagnetic Resonance SpectroscopyMembrane PotentialsMiceMice, Inbred C57BLCalcium ChannelsRecombinant ProteinsSynaptotagmin I

Identifiers

PMID16525042
PMCPMC6675161
OpenAlexW2026858216

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.